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Merck
CN

A6680

N-Acetylneuraminic Acid Aldolase from microorganisms

lyophilized powder, ≥20 units/mg protein (biuret)

Synonym(s):

N-Acetylneuraminate Pyruvate Lyase, N-Acetylneuraminic Acid Lyase, NANA Aldolase, Sialic Aldolase

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About This Item

CAS Number:
9027-60-5
NACRES:
NA.32
UNSPSC Code:
12352204
Beilstein/REAXYS Number:
2697172
MDL number:
MFCD00131656
EC Number:
4.1.3.3 (BRENDA, IUBMB)

Key Documents

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Product Name

N-Acetylneuraminic Acid Aldolase from microorganisms, lyophilized powder, ≥20 units/mg protein (biuret)

form

lyophilized powder

specific activity

≥20 units/mg protein (biuret)

mol wt

~98 kDa

storage temp.

−20°C

Quality Level

200

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Other Notes

One unit will release 1.0 μmole of pyruvate from NANA per min at pH 7.7 at 37 °C.

Physical form

Lyophilized powder containing mannitol and EDTA

Application

This enzyme is useful for enzymatic determination of N-acetylneuraminic acid and sialic acid when
coupled with the related enzymes in clinical analysis.
For industrial use, this enzyme is useful for enzymatic synthesis of sialic acid.
Used in the Sialic Acid Quantification Kit, SIALIC-Q

General description

Isoelectric point: 4.6 ± 0.1
Michaelis constant: 2.5 x 10‾3M (N-Acetylneuraminic acid)
Structure: 3 subunits (approx. 35,000) per mol of enzyme
Inhibitors: p-Chloromercuribenzoate, sodium dodecyl sulfact, Hg++, Ag+
Optimum pH: 7.5– 8.0
Optimum temp: 70°C
pH Stability: pH 6.0–9.0 (10°C, 25hr)
Thermal stability: Below 65°C (pH 7.5, 30 min)

Storage Class

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
SLCG9739
SLCB1930
SLBX5542
SLBS0864V
SLBJ8903V

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Vera Zimmermann et al.
Applied microbiology and biotechnology, 76(3), 597-605 (2007-07-03)
In this work, a model describing the complete enzyme catalysed synthesis of N-acetylneuraminic acid (Neu5Ac) from N-acetyl-D-glucosamine (GlcNAc) is presented. It includes the combined reaction steps of epimerisation from GlcNAc to N-acetyl-D-mannosamine (ManNAc) and the aldol condensation of ManNAc with
Hee Gon Jeong et al.
Infection and immunity, 77(8), 3209-3217 (2009-06-03)
N-acetylneuraminic acid (Neu5Ac, sialic acid) could provide a good substrate for enteropathogenic bacteria in the intestine, when the bacteria invade and colonize in human gut. In order to analyze the role of Neu5Ac catabolism in Vibrio vulnificus pathogenesis, a mutant
Jozef Nahálka et al.
Journal of biotechnology, 134(1-2), 146-153 (2008-03-04)
The propensity of a recombinant protein produced in bacteria to aggregate has been assumed to be unpredictable, and inclusion bodies have been thought of as wasted cell material. However, a target protein can be purposely driven to inclusion bodies, which
Yanhong Li et al.
Applied microbiology and biotechnology, 79(6), 963-970 (2008-06-04)
Sialic acid aldolases or N-acetylneuraminate lyases (NanAs) catalyze the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac) to form pyruvate and N-acetyl-D: -mannosamine (ManNAc). A capillary electrophoresis assay was developed to directly characterize the activities of NanAs in both Neu5Ac cleavage
Varun Bhaskar et al.
Proteins, 79(4), 1132-1142 (2011-02-05)
YagE is a 33 kDa prophage protein encoded by CP4-6 prophage element in Escherichia coli K12 genome. Here, we report the structures of YagE complexes with pyruvate (PDB Id 3N2X) and KDGal (2-keto-3-deoxy galactonate) (PDB Id 3NEV) at 2.2A resolution.
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